pyrularia/protease

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NakalaMajaribio ya klinikiHati miliki

Chagua aina ya aina

2 matokeo

Characterization and structural role of disulfide bonds in a highly knotted thionin from Pyrularia pubera.

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Ingia / Ingia

Disulfide bonds play a crucial role in the stabilization of the amphipathic folding of the diverse families of cysteine-rich antimicrobial peptides. The determination of cysteine pairings in these peptides has largely depended on sequence homology criteria, since the classical methods of disulfide

Role of Tyr and Trp in membrane responses of Pyrularia thionin determined by optical and NMR spectra following Tyr iodination and Trp modification.

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Ingia / Ingia

Pyrularia thionin is a strongly basic and bioactive 47 amino acid peptide which contains two Tyr residues at positions 13 and 45 and one Trp at position 8. Limited iodination does not have a significant effect, but prolonged iodination of the peptide leads to progressive inactivation for all known

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Herbal & Natural Medicine

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